PFF1_TALSN
ID PFF1_TALSN Reviewed; 985 AA.
AC B8M853;
DT 27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 51.
DE RecName: Full=Vacuolar membrane protease {ECO:0000250|UniProtKB:P38244};
DE EC=3.4.-.- {ECO:0000305};
DE AltName: Full=FXNA-related family protease 1 {ECO:0000250|UniProtKB:P38244};
GN ORFNames=TSTA_032680;
OS Talaromyces stipitatus (strain ATCC 10500 / CBS 375.48 / QM 6759 / NRRL
OS 1006) (Penicillium stipitatum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Trichocomaceae; Talaromyces;
OC Talaromyces sect. Talaromyces.
OX NCBI_TaxID=441959;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10500 / CBS 375.48 / QM 6759 / NRRL 1006;
RX PubMed=25676766; DOI=10.1128/genomea.01559-14;
RA Nierman W.C., Fedorova-Abrams N.D., Andrianopoulos A.;
RT "Genome sequence of the AIDS-associated pathogen Penicillium marneffei
RT (ATCC18224) and its near taxonomic relative Talaromyces stipitatus
RT (ATCC10500).";
RL Genome Announc. 3:E0155914-E0155914(2015).
CC -!- FUNCTION: May be involved in vacuolar sorting and osmoregulation.
CC {ECO:0000250|UniProtKB:P38244}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:P80561};
CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250|UniProtKB:P80561};
CC -!- SUBCELLULAR LOCATION: Vacuole membrane {ECO:0000250|UniProtKB:P38244};
CC Multi-pass membrane protein {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the peptidase M28 family. {ECO:0000305}.
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DR EMBL; EQ962654; EED20015.1; -; Genomic_DNA.
DR RefSeq; XP_002480449.1; XM_002480404.1.
DR AlphaFoldDB; B8M853; -.
DR SMR; B8M853; -.
DR STRING; 441959.B8M853; -.
DR EnsemblFungi; EED20015; EED20015; TSTA_032680.
DR GeneID; 8105007; -.
DR VEuPathDB; FungiDB:TSTA_032680; -.
DR eggNOG; KOG2194; Eukaryota.
DR HOGENOM; CLU_006412_1_0_1; -.
DR InParanoid; B8M853; -.
DR OMA; IHRFTYH; -.
DR OrthoDB; 166108at2759; -.
DR PhylomeDB; B8M853; -.
DR Proteomes; UP000001745; Unassembled WGS sequence.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005774; C:vacuolar membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008235; F:metalloexopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR InterPro; IPR045175; M28_fam.
DR InterPro; IPR007484; Peptidase_M28.
DR PANTHER; PTHR12147; PTHR12147; 1.
DR Pfam; PF04389; Peptidase_M28; 1.
PE 3: Inferred from homology;
KW Glycoprotein; Hydrolase; Membrane; Metal-binding; Metalloprotease;
KW Protease; Reference proteome; Transmembrane; Transmembrane helix; Vacuole;
KW Zinc.
FT CHAIN 1..985
FT /note="Vacuolar membrane protease"
FT /id="PRO_0000411744"
FT TOPO_DOM 1..16
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 17..37
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 38..383
FT /note="Vacuolar"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 384..404
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 405..438
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 439..459
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 460..469
FT /note="Vacuolar"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 470..490
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 491..500
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 501..521
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 522..525
FT /note="Vacuolar"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 526..546
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 547..659
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 660..680
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 681..696
FT /note="Vacuolar"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 697..717
FT /note="Helical; Name=8"
FT /evidence="ECO:0000255"
FT TOPO_DOM 718..726
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT TRANSMEM 727..747
FT /note="Helical; Name=9"
FT /evidence="ECO:0000255"
FT TOPO_DOM 748..985
FT /note="Vacuolar"
FT /evidence="ECO:0000250|UniProtKB:P38244"
FT REGION 586..606
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 614..633
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 212
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P80561"
FT BINDING 166
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P80561"
FT BINDING 178
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P80561"
FT BINDING 178
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P80561"
FT BINDING 213
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P80561"
FT BINDING 238
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P80561"
FT BINDING 311
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:P80561"
FT SITE 310
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:P80561"
FT CARBOHYD 113
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 116
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 791
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 985 AA; 109430 MW; 6C6581E2E0EA19D2 CRC64;
MARLRTGRWN PFAFYRVPVT VVITLIYIAL LAPLIVVQHV LPSVPESNPE GLDLLEAWRD
LQSLTNGFHP YNSRKNDEVR SWLLTRIDEI ISTNAAETLT RHDSARTFVF DDNQSNLTVV
ESNLGVYFEG TNIIVYVRGQ EDDKREWWNE PGLAPSGKGG VLVNAHYDSV STGYGATDDG
VGVISCLQLI KYFTTPGHEP LRGLVVLFNN GEEDFLNGAR VYSQHPISKL PHTFLNLEGA
GAGGRATLFR SSDTEVTKFY KRSPYPFGSV FSDAGFKLGL IRSETDYVIF EGDMGLRGLD
VAFIEPRARY HTNQDDAKHT SQQSLWHMLS AAVATTEGLV SDTSRDFEGR PQGPGKVPSG
TGSGAVWFDL FGTAFAVFQL HTLFALSVTL LIVGPLTLLI TSIILANQDR MYLFGISVSA
DDGFASVPLR GWRGFFRFPF IFGSTTASVV GLAFLMAKIN PMIAHSSEYA VWSMMISAWI
FVAWFLSRIA NFARPTALHR IYVLTWMFLL AWVLLVITTV YENRDGIASG YFVIFYAFGT
FLATWISYLE LFSLPKRSDY ANKFSGQISS RRTSLGGSRL LTPNPDFAGQ HQEDDEPTES
TSLLRSQRTS FANYTRSAED DGEGDLLSTG VGTDESEARD ANVYGYEQPW SANLPKWTWI
LQFLLIAPII TILVGQLGLL ITSAIHQTMQ DGSSALAPYL MIAIFTTLIF MPTLPFIHRY
TYHIPTFLLL VFIATLIYNL VAFPFSGNNR IKLFFLQEVD LDTGANRVSL TGILPFVDDA
AASIPSANGQ NISCIPKGDR TECSWESDLI PHVITHPGSG KQQTPMNEWV KYKAIRLEPG
RQNTNRAQFK ISGLNTRGCL LHFDKPISQF HVAGSATDSR FPSNPSLEDG TEDGVREIRL
WSRIWGNEWV IDVEWASHNN NNNNNNDDSD GGKDTLTGKA TCLWSDANTQ GTIPALDEVI
QYTPEWVAIT KLDAGLVKGS RSFEV
